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1W8E

3D structure of CotA incubated with hydrogen peroxide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0030435biological_processsporulation resulting in formation of a cellular spore
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A1512
ChainResidue
AHIS419
ACYS492
AHIS497
AMET502

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A1513
ChainResidue
AHIS107
AHIS153
AHIS493
APER1516

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A1514
ChainResidue
AHIS424
AHIS491
APER1516
AHIS155

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU A1515
ChainResidue
AHIS105
AHIS107
AHIS422
AHIS424
APER1516
AHOH2155

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PER A1516
ChainResidue
AHIS105
AHIS107
AHIS153
AHIS155
AHIS422
AHIS424
AHIS491
AHIS493
ACU1513
ACU1514
ACU1515
AHOH2449

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A1517
ChainResidue
AASP113
AASP114
ATYR118
AALA121
ATYR133
ALYS135
AHOH2171

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A1518
ChainResidue
ALYS25
ATYR69
AVAL138
ATHR307
AALA308
ATYR309
AGLU310
AGOL1519
AHOH2450

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A1519
ChainResidue
AARG136
AGLU137
AVAL138
ATHR307
AGLU310
AGOL1518
AHOH2282

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: type 2 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:14764581, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W6W, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:3ZDW
ChainResidueDetails
AHIS105
AHIS422

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: type 3 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:14764581, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0000269|PubMed:27050268, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W6W, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:3ZDW, ECO:0007744|PDB:4YVN, ECO:0007744|PDB:4YVU
ChainResidueDetails
AHIS107
AHIS153
AHIS155
AHIS424
AHIS491
AHIS493

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: type 1 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:14764581, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0000269|PubMed:27050268, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W6W, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:3ZDW, ECO:0007744|PDB:4YVN, ECO:0007744|PDB:4YVU
ChainResidueDetails
AHIS419
ACYS492
AHIS497

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: type 1 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0000269|PubMed:27050268, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:4YVN, ECO:0007744|PDB:4YVU
ChainResidueDetails
AMET502

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Plays a crucial role in the protonation steps => ECO:0000305|PubMed:22481612
ChainResidueDetails
AASP116

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Plays a crucial role in the protonation steps => ECO:0000305|PubMed:20200715, ECO:0000305|PubMed:20822511, ECO:0000305|PubMed:22481612
ChainResidueDetails
AGLU498

218853

PDB entries from 2024-04-24

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